Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents

Mihye Lee, Jihyun Shim, Philjae Kang, Moon Gun Choi, Soo Hyuk Choi

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


α/β-Peptides with alternating α-amino acid and cis-2-aminocyclohexanecarboxylic acid (cis-ACHC) residues adopt 11/9-helical conformations, the folding propensity of which decreases as the solvent polarity increases. We report a new cis-ACHC analogue, cis-2-amino-cis-4-methylcyclohexanecarboxylic acid, which significantly stabilizes the 11/9-helix propensity in protic solvents.

Original languageEnglish
Pages (from-to)5950-5952
Number of pages3
JournalChemical Communications
Issue number35
Publication statusPublished - 2016 May 1

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry 2016.

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • General Chemistry
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry


Dive into the research topics of 'Stabilization of 11/9-helical α/β-peptide foldamers in protic solvents'. Together they form a unique fingerprint.

Cite this